VME1_CVMA5
ID VME1_CVMA5 Reviewed; 228 AA.
AC P03415;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Membrane protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE Short=M protein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=E1 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Matrix glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
DE AltName: Full=Membrane glycoprotein {ECO:0000255|HAMAP-Rule:MF_04202};
GN Name=M {ECO:0000255|HAMAP-Rule:MF_04202}; ORFNames=6;
OS Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11142;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6325918; DOI=10.1038/308751a0;
RA Armstrong J., Niemann H., Smeekens S., Rottier P.J.M., Warren G.;
RT "Sequence and topology of a model intracellular membrane protein, E1
RT glycoprotein, from a coronavirus.";
RL Nature 308:751-752(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6331107; DOI=10.1007/978-1-4615-9373-7_16;
RA Armstrong J., Smeekens S., Spaan W.J.M., Rottier P.J.M.,
RA van der Zeijst B.A.M.;
RT "Cloning and sequencing the nucleocapsid and E1 genes of coronavirus.";
RL Adv. Exp. Med. Biol. 173:155-162(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate C12 mutant;
RX PubMed=9426441; DOI=10.1006/viro.1997.8877;
RA Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.;
RT "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
RT associated with a Q159L amino acid substitution in the spike protein.";
RL Virology 239:1-10(1997).
RN [4]
RP TOPOLOGY.
RX PubMed=1400501; DOI=10.1016/s0021-9258(19)36699-2;
RA Locker J.K., Rose J.K., Horzinek M.C., Rottier P.J.M.;
RT "Membrane assembly of the triple-spanning coronavirus M protein. Individual
RT transmembrane domains show preferred orientation.";
RL J. Biol. Chem. 267:21911-21918(1992).
RN [5]
RP INTERACTION WITH S, AND MUTAGENESIS OF TYR-211.
RX PubMed=10438834; DOI=10.1128/jvi.73.9.7441-7452.1999;
RA de Haan C.A.M., Smeets M., Vernooij F., Vennema H., Rottier P.J.M.;
RT "Mapping of the coronavirus membrane protein domains involved in
RT interaction with the spike protein.";
RL J. Virol. 73:7441-7452(1999).
RN [6]
RP HOMOTYPIC INTERACTION, AND MUTAGENESIS OF 2-SER-SER-3 AND 225-LEU-LEU-226.
RX PubMed=10799570; DOI=10.1128/jvi.74.11.4967-4978.2000;
RA de Haan C.A.M., Vennema H., Rottier P.J.M.;
RT "Assembly of the coronavirus envelope: homotypic interactions between the M
RT proteins.";
RL J. Virol. 74:4967-4978(2000).
RN [7]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=1629209; DOI=10.1016/s0021-9258(19)49683-x;
RA Locker J.K., Griffiths G., Horzinek M.C., Rottier P.J.M.;
RT "O-glycosylation of the coronavirus M protein. Differential localization of
RT sialyltransferases in N- and O-linked glycosylation.";
RL J. Biol. Chem. 267:14094-14101(1992).
CC -!- FUNCTION: Component of the viral envelope that plays a central role in
CC virus morphogenesis and assembly via its interactions with other viral
CC proteins. {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBUNIT: Homomultimer. Interacts with envelope E protein in the budding
CC compartment of the host cell, which is located between endoplasmic
CC reticulum and the Golgi complex. Forms a complex with HE and S
CC proteins. Interacts with nucleocapsid N protein. This interaction
CC probably participates in RNA packaging into the virus.
CC {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000255|PROSITE-
CC ProRule:PRU01275}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04202}. Note=Largely embedded in the lipid bilayer.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
CC -!- PTM: O-linked glycans consist of Gal-GalNAc disaccharides which are
CC modified with up to 2 sialic acid residues (done in recombinantly
CC expressed E1 glycoprotein in SAC(-) cells infected with recombinant
CC vaccinia vector).
CC -!- SIMILARITY: Belongs to the betacoronaviruses M protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04202}.
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DR EMBL; X00509; CAA25197.1; -; Genomic_RNA.
DR EMBL; M25894; AAA46452.1; -; Genomic_RNA.
DR EMBL; AF029248; AAB86822.1; -; Genomic_RNA.
DR PIR; A04020; VGIHE1.
DR RefSeq; NP_045301.1; NC_001846.1.
DR SMR; P03415; -.
DR GlyConnect; 123; 6 O-Linked glycans.
DR GeneID; 1489756; -.
DR KEGG; vg:1489756; -.
DR Proteomes; UP000007192; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IDA:CACAO.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule.
DR CDD; cd21568; HCoV-like_M; 1.
DR HAMAP; MF_04202; BETA_CORONA_M; 1.
DR InterPro; IPR002574; M_CoV.
DR InterPro; IPR044362; M_HCoV-like.
DR Pfam; PF01635; CoV_M; 1.
DR PROSITE; PS51927; COV_M; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral immunoevasion; Viral matrix protein; Virion.
FT CHAIN 1..228
FT /note="Membrane protein"
FT /id="PRO_0000106037"
FT TOPO_DOM 2..25
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 47..56
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 78..85
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT TOPO_DOM 107..228
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04202"
FT MUTAGEN 2..3
FT /note="SS->AA: Does not affect the ability to interact with
FT itself."
FT /evidence="ECO:0000269|PubMed:10799570"
FT MUTAGEN 211
FT /note="Y->G: Abolishes the ability to form virus-like
FT particles. Does not abolish the interaction with S
FT protein."
FT /evidence="ECO:0000269|PubMed:10438834"
FT MUTAGEN 225..226
FT /note="LL->KK: Does not affect the ability to interact with
FT itself."
FT /evidence="ECO:0000269|PubMed:10799570"
SQ SEQUENCE 228 AA; 26027 MW; 962D82A184248CFA CRC64;
MSSTTQAPEP VYQWTADEAV QFLKEWNFSL GIILLFITII LQFGYTSRSM FIYVVKMIIL
WLMWPLTIVL CIFNCVYALN NVYLGFSIVF TIVSIVIWIM YFVNSIRLFI RTGSWWSFNP
ETNNLMCIDM KGTVYVRPII EDYHTLTATI IRGHLYMQGV KLGTGFSLSD LPAYVTVAKV
SHLCTYKRAF LDKVDGVSGF AVYVKSKVGN YRLPSNKPSG ADTALLRI
